ID A0A1J9QL59_9EURO Unreviewed; 1131 AA.
AC A0A1J9QL59;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN ORFNames=AJ78_03252 {ECO:0000313|EMBL:OJD16612.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD16612.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD16612.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD16612.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
CC {ECO:0000256|ARBA:ARBA00008695}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJD16612.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGRN01000100; OJD16612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9QL59; -.
DR STRING; 1447872.A0A1J9QL59; -.
DR VEuPathDB; FungiDB:AJ78_03252; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000182235; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16023; GPI_EPT_3; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037675; PIG-O_N.
DR InterPro; IPR039524; PIGO/GPI13.
DR PANTHER; PTHR23071:SF1; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 3; 1.
DR PANTHER; PTHR23071; PHOSPHATIDYLINOSITOL GLYCAN; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000182235};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 660..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 758..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 988..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 123892 MW; 53AB0329AB12911A CRC64;
MKPAASASKN AIRSKQSLTS QSQPQSPAST NEFQNIKAQW ASAKALAEEE QAQKVAAAER
IKQRVSMGVD VGAGAGDKTR EEALIKAAKE MDMQRNKVKE SVFKIEHAGV LGVLGWFLFI
HLVGIYFFTK GFLLSRTVLE NKSECTVLPF DGAAADSSQV SDQGCWHPKT FDKAIVIIID
ALRYDFTVPF RPTVEGQLPH LFHNNFPVLY ETAVESPEKA FLLPFIADPP TTTLQRLKGL
TTGTLPTFIE AGSNFAGTAI DEDNLIAQLH NAGKRIVHLG DDTWQSLFPD LFEPKLSHPY
DSFNVRDLHT VDNGVTEHLF PLLHADNATK WDVVVGHYLG VDHAGHRYGP NHAATAAKLH
QMDQVIRDVI KSIDGSTLLV VMGDHGMDGK GDHGGESDDE VEAALWMYSK RGVFGRPNSA
TLEPPRTAKE RPIPQIDLVP TLALLLGMPI PFNNLGSPIE EAFSGADGRD LKNLVRVNRL
ASAQINQYQR EYALISGVDQ SHTSGPLGIW SRAEEDWDSI SQHQHRSSNL DRPVLQKVYD
SYREYQRDTL RVCKGMWAKF DIPSMIQGIL ILFAGIVLLV FYARGICGDL TDLSFPTLRR
VGVGSGVGVI GGMILTGIGI AKLSRVEGLV LGIAVGGLFA ASSTVLWVPK RIVSPLPNSL
WAWLAVVFTA SQSVGFASNS YTVWEDEILL YFLTTFGVLA ALSSLRQKRT EDRVLGFYHS
IVFVFLGRLA SLSRLCREEQ IPSCVSTYYA SSTSSTSAWW QLFIPFLLAV FLPSVIRSYY
RGTKSYEGSA VFWIGIAFRT GLFIVAVFWT LDAADDGDWF PSLSKTLVKT TRIVLAQIVL
AIAFAAGTTT FGWAKPCINV AMTPDPSNPA TPTLQQPPRK TIVTILGYAN IHGTRYALLL
INFALAIILL QKPMGGGAIG LQTWQIFSLL EILDTNGLTS KSAIGPVVLG LLGSFHFFTT
GHQATLSSIQ WKIAFVPLTT VKYPWSPLII VLNTFGAQIL SAIAVPLTVL WKRPIDARSG
PLSQTSSIQG RAQTEGQPPA ASQPSKNRAS RILSDVVQAA TTHILYYATI NLATTMWAGW
LRRHLMLYRI FSPRFMMGAV VLGVVDVVVL FVSVAGVRWS TVSVGEVFGW S
//
